Cited by 828Advanced Glycation End Products researchPotato Plant ResearchAntioxidant Activity and Oxidative Stress

Advanced glycoxidation and lipoxidation end products (AGEs and ALEs): An overview of their mechanisms of formation

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Vistoli, G., De Maddis, D., Cipak, A., Zarkovic, N., Carini, M., Aldini, G.·2013·Free Radical Research

Abstract

Advanced lipoxidation end products (ALEs) and advanced glycation end products (AGEs) have a pathogenetic role in the development and progression of different oxidative-based diseases including diabetes, atherosclerosis, and neurological disorders. AGEs and ALEs represent a quite complex class of compounds that are formed by different mechanisms, by heterogeneous precursors and that can be formed either exogenously or endogenously. There is a wide interest in AGEs and ALEs involving different aspects of research which are essentially focused on set-up and application of analytical strategies (1) to identify, characterize, and quantify AGEs and ALEs in different pathophysiological conditions; (2) to elucidate the molecular basis of their biological effects; and (3) to discover compounds able to inhibit AGEs/ALEs damaging effects not only as biological tools aimed at validating AGEs/ALEs as drug target, but also as promising drugs. All the above-mentioned research stages require a clear picture of the chemical formation of AGEs/ALEs but this is not simple, due to the complex and heterogeneous pathways, involving different precursors and mechanisms. In view of this intricate scenario, the aim of the present review is to group the main AGEs and ALEs and to describe, for each of them, the precursors and mechanisms of formation.

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Crossref · 10.3109/10715762.2013.815348

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  • 4-Hydroxy-2-nonenal (4-HNE) forms stable Michael adducts with cysteine and histidine; nucleophilic attack of lysine forms unstable Michael adducts that require reduction prior to analysis.

    “This positive partial charge is attacked by nucleophiles such as cysteine and histidine and stable Michael adducts are formed (Fig. 4B) [50]. Nucleophilic attack of lysine forms unstable Michael adducts, which require reduction, e.g., by sodium borohydride prior to analysis [57].”

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Authors
Vistoli, G., De Maddis, D., Cipak, A., Zarkovic, N., Carini, M., & Aldini, G.
Affiliations
University of Milan (IT)
Corresponding author
Aldini, G.
Venue
Free Radical Research
Published
2013-06-17
Volume
47
Issue
sup1
Pages
3-27
ISSN
  • 1029-2470 (ISSN-L)
  • 1071-5762
OpenAlex
W2136497849
Cited by
823
References
247
Citations by year
2026: 38 · 2025: 58 · 2024: 84 · 2023: 85 · 2022: 96 · 2021: 84 · 2020: 68 · 2019: 69 · 2018: 61 · 2017: 64 · 2016: 41 · 2015: 37 · 2014: 31 · 2013: 3
FWCI
3.86
Type
journal article
Language
en
Open access
Locations
  • Free Radical Research (publishedVersion)
  • PubMed (publishedVersion)
  • Institutional Repository of the Ruđer Bošković Institute (Ruđer Bošković Institute) (submittedVersion, other-oa)
Funders
Ministero dell'Università e della Ricerca
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Advanced Glycation End Products research
  • Life Sciences › Agricultural and Biological Sciences › Food Science › Potato Plant Research
  • Health Sciences › Medicine › Biochemistry › Antioxidant Activity and Oxidative Stress
Keywords
advanced glycation end products, advanced lipoxidation end products, oxidative stress, diabetes mellitus, atherosclerosis, neurological disorders, AGE inhibitors
MeSH terms
Receptor for Advanced Glycation End Products, Humans, Pyruvaldehyde, Receptors, Immunologic, Lipid Peroxidation, Maillard Reaction, Glycation End Products, Advanced, Protein Carbonylation

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